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Zinc in PDB 7q29: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013

Enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013, PDB code: 7q29 was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 66.36 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.164, 84.765, 132.728, 90, 90, 90
R / Rfree (%) 16.1 / 18.4

Other elements in 7q29:

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013 (pdb code 7q29). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013, PDB code: 7q29:

Zinc binding site 1 out of 1 in 7q29

Go back to Zinc Binding Sites List in 7q29
Zinc binding site 1 out of 1 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain in Complex with Dual Ace/Nep Inhibitor AD013 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn713

b:11.8
occ:1.00
 OE1 A:GLU411 1.9 10.8 1.0
O31 A:8JV707 2.0 15.7 1.0
NE2 A:HIS387 2.0 11.1 1.0
NE2 A:HIS383 2.0 11.4 1.0
O01 A:8JV707 2.6 15.6 1.0
C02 A:8JV707 2.6 14.3 1.0
CD A:GLU411 2.9 12.0 1.0
CE1 A:HIS387 2.9 13.4 1.0
CE1 A:HIS383 2.9 13.9 1.0
HE1 A:HIS387 3.0 16.1 1.0
CD2 A:HIS383 3.0 11.8 1.0
HE1 A:HIS383 3.1 16.7 1.0
CD2 A:HIS387 3.1 8.4 1.0
OE2 A:GLU411 3.2 11.7 1.0
HE1 A:TYR523 3.3 12.3 1.0
HD2 A:HIS383 3.3 14.1 1.0
HD2 A:HIS387 3.3 10.1 1.0
HH A:TYR523 3.6 12.9 1.0
HA A:GLU411 3.6 11.4 1.0
H051 A:8JV707 3.9 23.1 1.0
ND1 A:HIS383 4.0 13.1 1.0
ND1 A:HIS387 4.0 11.7 1.0
C03 A:8JV707 4.1 16.0 1.0
CG A:HIS383 4.1 10.5 1.0
CE1 A:TYR523 4.1 10.3 1.0
H11 A:PEG708 4.2 47.2 1.0
CG A:HIS387 4.2 9.0 1.0
CG A:GLU411 4.3 9.9 1.0
H242 A:8JV707 4.3 24.7 1.0
H141 A:8JV707 4.3 16.7 1.0
HB3 A:GLU411 4.3 11.0 1.0
H031 A:8JV707 4.3 19.1 1.0
OH A:TYR523 4.4 10.7 1.0
O A:HOH978 4.4 14.9 1.0
CA A:GLU411 4.5 9.5 1.0
O A:HOH1057 4.5 16.5 1.0
CB A:GLU411 4.6 9.2 1.0
OE2 A:GLU384 4.7 12.9 1.0
C05 A:8JV707 4.7 19.2 1.0
HG3 A:GLU411 4.7 11.8 1.0
CZ A:TYR523 4.8 11.4 1.0
HD1 A:HIS383 4.8 15.7 1.0
HD1 A:HIS387 4.8 14.0 1.0
N04 A:8JV707 4.8 20.1 1.0
H1 A:8JV707 4.8 24.2 1.0
HG2 A:GLU411 4.8 11.8 1.0
OE1 A:GLU384 4.9 12.9 1.0
C23 A:8JV707 5.0 17.9 1.0
H231 A:8JV707 5.0 21.4 1.0
H132 A:8JV707 5.0 22.9 1.0

Reference:

L.B.Arendse, G.E.Cozier, C.J.Eyermann, G.S.Basarab, S.L.Schwager, K.Chibale, K.R.Acharya, E.D.Sturrock. Probing the Requirements For Dual Angiotensin-Converting Enzyme C-Domain Selective/Neprilysin Inhibition. J.Med.Chem. V. 65 3371 2022.
ISSN: ISSN 0022-2623
PubMed: 35113565
DOI: 10.1021/ACS.JMEDCHEM.1C01924
Page generated: Wed Oct 30 09:33:53 2024

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